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Influence of Human Serum Albumin on Photodegradation of Folic Acid in Solution
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ABSTRACTIt has been proposed that photodegradation of folates may be the reason for the pigmentation of races living under high fluence rates of ultraviolet radiation. The photodegradation of folic acid (FA) induced by ultraviolet‐A (UV‐A) radiation, in solution and in the presence of human serum albumin (HSA), was studied with absorption and fluorescence spectroscopy. FA photodegradation, with formation of p‐aminobenzoyl‐L‐glutamic acid, 6‐formylpterin and pterin‐6‐carboxylic acid, was found to follow an exponential trend. A scheme of FA photodegradation, which involves photosensitization of FA degradation by its photoproducts, was proposed. The rate of FA photodegradation decreased drastically in the presence of HSA, whereas the spectral characteristics of the photo‐products remained constant. The reduction of the FA photo‐degradation rate by HSA was accompanied by degradation of tryptophan in HSA. Tryptophan, when added to solutions of FA, had a similar effect as HSA. In solutions of FA and HSA the FA photoproducts cause photodamage mainly to HSA rather than to FA itself. The oxygen dependence of FA photo‐degradation and the inhibition of this process by sodium azide indicate that singlet oxygen may participate in the photosensitizing activity of FA photoproducts.
Title: Influence of Human Serum Albumin on Photodegradation of Folic Acid in Solution
Description:
ABSTRACTIt has been proposed that photodegradation of folates may be the reason for the pigmentation of races living under high fluence rates of ultraviolet radiation.
The photodegradation of folic acid (FA) induced by ultraviolet‐A (UV‐A) radiation, in solution and in the presence of human serum albumin (HSA), was studied with absorption and fluorescence spectroscopy.
FA photodegradation, with formation of p‐aminobenzoyl‐L‐glutamic acid, 6‐formylpterin and pterin‐6‐carboxylic acid, was found to follow an exponential trend.
A scheme of FA photodegradation, which involves photosensitization of FA degradation by its photoproducts, was proposed.
The rate of FA photodegradation decreased drastically in the presence of HSA, whereas the spectral characteristics of the photo‐products remained constant.
The reduction of the FA photo‐degradation rate by HSA was accompanied by degradation of tryptophan in HSA.
Tryptophan, when added to solutions of FA, had a similar effect as HSA.
In solutions of FA and HSA the FA photoproducts cause photodamage mainly to HSA rather than to FA itself.
The oxygen dependence of FA photo‐degradation and the inhibition of this process by sodium azide indicate that singlet oxygen may participate in the photosensitizing activity of FA photoproducts.
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